Molecular plasticity of CBM3 ancillary domain leads to conformational changes in the cellulose binding interface

Autor(es)

Morais, Mariana Abrahao Bueno ; Paiva, Joice Helena ; Murakami, Mario Tyago

• Tipo de documento: Artigo Científico
• Fonte: Biochemical and Biophysical Research Communications; v. 645, p. 8-pg., 2023-01-19.

Resumo

Carbohydrate-binding modules (CBMs) constitute independently folded domains typically associated with carbohydrate-active enzymes (CAZymes). These modules are considered to have a rigid structure without notable conformational changes upon ligand binding, exhibiting a complementary topography in relation to the target carbohydrate. Herein, the high-resolution SAD-solved structure of a CBM from family 3 (BsCBM3) that binds to crystalline cellulose is reported in two crystalline forms. This module showed molecular plasticity with structural differences detected between the two crystalline forms and high RMSD values when compared to NMR ensemble of models. Pronounced structural variances were observed in the cellulose binding interface between NMR and XTAL structures, which were corroborated by molecular dynamics simulations. These findings support that family 3 CBMs targeting to cellulose are rather structurally dynamic modules than rigid entities, suggesting a potential role of conformational changes in polysaccharide recognition and modulation of enzyme activity. (c) 2023 Elsevier Inc. All rights reserved. (AU)

• Processo FAPESP: 08/10555-1 - Caracterização estrutural da proteína efetora PthA de Xanthomonas axonopodis pv. citri, agente causal do cancro cítrico
• Beneficiário: Joice Helena Paiva
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 16/19995-0 - Análise da diversidade estrutural e funcional das enzimas pertencentes à família GH43 em Xanthomonas axonopodis pv. citri: implicações biológicas e possíveis aplicações biotecnológicas
• Beneficiário: Mariana Abrahão Bueno de Morais
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 15/26982-0 - Explorando novas estratégias para a despolimerização de polissacarídeos da parede celular vegetal: da estrutura, função e desenho racional de hidrolases glicosídicas às implicações biológicas e potenciais aplicações biotecnológicas
• Beneficiário: Mário Tyago Murakami
• Modalidade de apoio: Auxílio à Pesquisa - Temático